Research workbench
Crystal structure of a glutathione transferase family member from ricinus communis, target efi-501866
Analyse Crystal structure of a glutathione transferase family member from ricinus… in the GL1X research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides, crosslinks and neighbours on the 3D structure.
- PDB
- 4J2F
- Type
- protein
- Length
- 218 residues
- Chains
- 1
- Method
- x-ray diffraction
- Collection
- MolNFT v1 / PDB
- Contract
- 0xDE3723766Bc32dcACD03C17BaA400A7B36837Eba
- Owner
- 0x3396CDB397284571d12822B4ae1189a8E22AAAAA
- Molecule
- Glutathione S-transferase
- EC
- 4.4.1.5
- UniProt
- B9RWR5
- Pockets
- 2 · best druggability 0.62
Structure
x-ray diffraction · 1 distinct chain · 56% helix, 9% strand (DSSP).
| Chain | Molecule | Type | Residues | Secondary structure | UniProt |
|---|---|---|---|---|---|
| A | Glutathione S-transferase (EC 4.4.1.5) | protein | 218 | 56% helix, 9% strand | B9RWR5 |
Ligands and binding sites
- GOL · Glycerol · additive · chains A
Binding sites are the residues within 4.5 Å of a ligand's heavy atoms.
Pockets
2 pockets found on a 1 Å grid, 1 with a druggability of 0.5 or more.
| Volume (ų) | Druggability | Buriedness | Lining residues | Inside | |
|---|---|---|---|---|---|
| 1 | 338 | 0.62 | 0.78 | 37 | empty |
| 2 | 169 | 0.48 | 0.77 | 33 | empty |
Compared structures
- 4J2F · Crystal structure of a glutathione transferase family member from Ricinus communis… · the same entry in another collection · chain A against A, TM-score 1.00
Analyse
- Open in the research workbench: secondary structure, accessibility, pockets, interfaces, conservation, variants, modifications, peptides and crosslinks on the 3D structure
- Every structure of UniProt B9RWR5
- Elsewhere: RCSB PDB 4J2F · PDBe 4J2F · UniProt B9RWR5
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